1.
Proteins
; 85(5): 951-956, 2017 05.
Artigo
em Inglês
| MEDLINE
| ID: mdl-28160315
RESUMO
We report the solution NMR structure of RHE_CH02687 from Rhizobium etli. Its structure consists of two ß-sheets that together with two short and one long α-helix form a hydrophobic cavity. This protein shows a high structural similarity to the prokaryotic protein YndB from Bacillus subtilis, and the eukaryotic protein Aha1. NMR titration experiments confirmed that RHE_CH02687, like its homolog YndB, interacted with flavonoids, giving support for a biological function as a flavonoid sensor in the symbiotic interaction between R. etli and plants. In addition, our study showed no evidence for a direct interaction between RHE_CH02687 and HtpG, the R. etli homolog of Hsp90. Proteins 2017; 85:951-956. © 2016 Wiley Periodicals, Inc.